Turnover of oxidatively modified proteins: the usage of in vitro and metabolic labeling.
Cellular reactions to oxidative stress always include a response in the protein turnover. Therefore, cellular handling of proteins is important to observe. In this method review, radioactive labeling of proteins in vitro and in intact cells is described. The use of techniques based on the radioactive quantification of amino acids is much more selective and reliable than other nonradioactive methods for studying the protein turnover of both long- and short-lived proteins. Variations of such measurements allow one to measure protein synthesis, protein degradation, formation of insoluble proteins, and, perhaps, the turnover of individual proteins.
Catalgol
Betul
B
Institute of Biological Chemistry and Nutrition, University Hohenheim, Stuttgart, Germany.
Grune
Tilman
T
D000596:Amino Acids / Q000378:metabolism; D000818:Animals; D001671:Biochemistry / Q000379:methods; D002457:Cell Extracts; D002477:Cells / Q000378:metabolism; D006801:Humans; D007553:Isotope Labeling / Q000379:methods; D046912:Multiprotein Complexes / Q000378:metabolism; D010084:Oxidation-Reduction; D011485:Protein Binding; D014176:Protein Biosynthesis; D011506:Proteins / Q000378:metabolism*; D011851:Radioactivity; D011868:Radioisotopes / Q000378:metabolism*; D012680:Sensitivity and Specificity
D000596:Amino Acids; D002457:Cell Extracts; D046912:Multiprotein Complexes; D011506:Proteins; D011868:Radioisotopes